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Literature summary extracted from

  • Lieder, K.W.; Booker, S.; Ruzicka, F.J.; Beinert, H.; Reed, G.H.; Frey, P.A.
    S-Adenosylmethionine-dependent reduction of lysine 2,3-aminomutase and observation of the catalytically functional iron-sulfur centers by electron paramagnetic resonance (1998), Biochemistry, 37, 2578-2585.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
5.4.3.2 S-adenosylmethionine required Clostridium subterminale
5.4.3.2 S-adenosylmethionine plays a role in lysine 2,3-aminomutase reaction Clostridium subterminale

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.4.3.2 Fe2+ role of the iron-sulfur clusters in the reaction Clostridium subterminale
5.4.3.2 Fe2+ Fe-S cluster is required as cofactor Clostridium subterminale

Organism

EC Number Organism UniProt Comment Textmining
5.4.3.2 Clostridium subterminale
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
5.4.3.2 L-lysine = (3S)-3,6-diaminohexanoate reaction proceeds by a substrate radical rearrangement mechanism, in which the external aldimine formed between pyridoxal phosphate and Lys is initially converted into a lysyl-radical intermediate by hydrogen abstraction from C3 Clostridium subterminale
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.3.2 L-Lys
-
 Clostridium subterminale (3S)-3,6-diaminohexanoic acid
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
5.4.3.2 pyridoxal 5'-phosphate required Clostridium subterminale
5.4.3.2 pyridoxal 5'-phosphate role in lysine 2,3-aminomutase reaction Clostridium subterminale